Unveiling the structural properties of the ATP Synthase subunit OSCP by SAXS

Gabriele Giachin.

SASDVR9 – C-terminal tail of human mitochondrial ATP synthase subunit O (137-213) (Oligomycin Sensitivity Conferral Protein or Complex V subunit O)

ATP synthase subunit O, mitochondrial C-terminal section
MWexperimental 24 kDa
MWexpected 25 kDa
VPorod 32 nm3
log I(s) 4.26×101 4.26×100 4.26×10-1 4.26×10-2
ATP synthase subunit O, mitochondrial C-terminal section small angle scattering data  s, nm-1
ln I(s)
ATP synthase subunit O, mitochondrial C-terminal section Guinier plot ln 4.26×101 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
ATP synthase subunit O, mitochondrial C-terminal section Kratky plot 1.104 0 √3 sRg
p(r)
ATP synthase subunit O, mitochondrial C-terminal section pair distance distribution function Rg: 2.1 nm 0 Dmax: 6.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
ATP synthase subunit O, mitochondrial C-terminal section ALPHAFOLD model
Synchrotron SAXS data from solutions of C-terminal tail of human mitochondrial ATP synthase subunit O (137-213) (Oligomycin Sensitivity Conferral Protein or Complex V subunit O) in 50 mM Na2HPO4, 300 mM NaCl, pH 7 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.50 mg/ml was measured at 20°C. 10 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

ATP synthase subunit O, mitochondrial C-terminal section
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Trimer
Mon. MW   8.3 kDa
 
UniProt   P48047 (137-213)
Sequence   FASTA